IHC image of CSB-PA010100OA04nme1HU diluted at 1:50 and staining in paraffin-embedded human melanoma performed on a Leica BondTM system. After dewaxing and hydration, antigen retrieval was mediated by high pressure in a citrate buffer (pH 6.0). Section was blocked with 10% normal goat serum 30min at RT. Then primary antibody (1% BSA) was incubated at 4°C overnight. The primary is detected by a biotinylated secondary antibody and visualized using an HRP conjugated SP system.

Immunofluorescence staining of Hela cells with CSB-PA010100OA04nme1HU at 1:2.5, counter-stained with DAPI. The cells were fixed in 4% formaldehyde, permeabilized using 0.2% Triton X-100 and blocked in 10% normal Goat Serum. The cells were then incubated with the antibody overnight at 4°C. The secondary antibody was Alexa Fluor 488-congugated AffiniPure Goat Anti-Rabbit IgG(H+L).

Chromatin Immunoprecipitation Hela (4*106) were treated with Micrococcal Nuclease, sonicated, and immunoprecipitated with 5µg anti-H2AFZ (CSB-PA010100OA04nme1HU) or a control normal rabbit IgG. The resulting ChIP DNA was quantified using real-time PCR with primers against the β-Globin promoter.

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Target Data

Function

Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. May be involved in the formation of constitutive heterochromatin. May be required for chromosome segregation during cell division.

Gene References into Functions

H2A.Z associates with epigenetic gene activation in prostate cancer.Acetylated H2A.Z role in activation of newly formed enhancers in prostate cancer. PMID: 29116202

The present study demonstrated that H2A.Z is overexpressed in ICC and expression of H2A.Z correlated with poor prognosis in patients with ICC. H2A.Z regulated cell proliferation in vitro and in vivo via H2A.Z/S-phase kinase-associated protein 2/p27/p21 signaling. PMID: 29532867

Two possible modes of pioneering associated with combinations of H2A.Z and p300/CBP at nucleosome-occupied enhancers. PMID: 28301306

Results indicate that accumulation of H2A.Z within repressed genes can also be a consequence of the repression of gene transcription rather than an active mechanism required to establish the repression. PMID: 29036442

Findings suggest the oncogenic potential of H2A.Z.1 in liver tumorigenesis and that it plays established role in accelerating cell cycle transition and EMT during hepatocarcinogenesis. PMID: 26863632

Crystal structure results show that the flexible character of the H2A.Z L1 loop plays an essential role in forming the stable heterotypic H2A.Z/H2A nucleosome. PMID: 27358293

H2A.Z removal from chromatin is the primary function of INO80 and ANP32E in promoting homologous recombination. PMID: 26142279

Results demonstrated male-selective association of the H2AFZ gene with schizophrenia, and that modification of the H2AFZ signaling pathway warrants further study in terms of the pathophysiology of schizophrenia PMID: 25392085

Dynamic modulation of H2A.Z exchange and removal by Anp32e reveals the importance of the nucleosome surface and nucleosome dynamics in processing the damaged chromatin template during DSB repair. PMID: 26034280

The findings implicate H2A.Z.2 as a mediator of cell proliferation and drug sensitivity in malignant melanoma. PMID: 26051178

the predictive values regarding low expressions of H2AFZ and CASP8AP2 and high white blood cell count suggest that these features could help to identify more accurately patients at greater risk of relapse. PMID: 24397596

Anp32e may help to resolve the non-nucleosomal H2A.Z aggregates and also facilitate the removal of H2A.Z at the +1 nucleosomes, and the latter may help RNA polymerase II to pass the first nucleosomal barrier. PMID: 24613878

Study mapped H2A.Z genome-wide in embryonic stem cells and neural progenitors; H2A.Z is deposited at promoters and enhancers, and correlates strongly with H3K4 methylation. H2A.Z is present at poised promoters with bivalent chromatin and at active promoters with H3K4 methylation, but is absent from stably repressed promoters that are enriched for H3K27 trimethylation. PMID: 23034477

Depletion of H2A.Z in the osteosarcoma U2OS cell line and in immortalized human fibroblasts does not change parameters of DNA double-strand breaks repair while affecting clonogenic ability and cell cycle distribution. PMID: 24240188

A mutational analysis revealed that the amino-acid difference at position 38 is at least partially responsible for the structural polymorphism in the L1 loop region of H2A.Z.1 and H2A.Z.2. PMID: 24311584

age-dependent p400 downregulation and loss of H2A.Z localisation may contribute to the onset of replicative senescence through a sustained high rate of p21 transcription PMID: 23146670

H2A.Z exchange promotes specific patterns of histone modification and reorganization of the chromatin architecture, leading to the assembly of a chromatin template that is an efficient substrate for the DNA double-strand break repair machinery. PMID: 23122415

ZNF24 may be implicated in transcriptional regulation of genes associated with oncogenesis via interaction with H2A.Z. PMID: 22678762

incorporation of the histone variant H2A.Z at the promoter regions of PPARgamma target genes by p400/Brd8 is essential to allow fat cell differentiation PMID: 23064015

The short forms of H2A.Z in both yeast and human cells are more loosely associated with chromatin than the full-length proteins, indicating a conserved function for the H2A.Z C-terminal tail in regulating the association of H2A.Z with nucleosomes. PMID: 22493515

acetylation of H2A.Z is a key modification associated with gene activity in normal cells and epigenetic gene deregulation in tumorigenesis. PMID: 21788347

H2A.Z is maintained during mitosis and marks the +1 nucleosome of active genes, which shifts during mitosis, resulting in occupancy at the transcriptional start site and a reduced nucleosome-depleted region. PMID: 20864037

This review provides a brief overview of H2A.Z biology and presents hypotheses that could reconcile contradictory reports that are found in the literature regarding the influence of H2A.Z on nucleosome stability. PMID: 20364108

chromatin remodeling at the c-myc gene involves the local exchange of histone H2A.Z PMID: 15878876

neither H2AZ itself nor other features of the H2AZ-containing nucleosome spread to the neighboring nucleosomes in vivo, arguing against a role for H2AZ as a self-perpetuating epigenetic mark PMID: 16809769

identify the essential histone variant H2A.Z as a new structural component of the centromere PMID: 17194760

Monoubiquitylation of H2A.z distinguishes its association with euchromatin or facultative heterochromatin. PMID: 17636032

Upon DNA damage, histone H2A.Z is first evicted from the p21 promoter, followed by the recruitment of the Tip60 histone acetyltransferase to activate p21 transcription. PMID: 17671089

Results show that H2A.Z nucleosomes protect only approximately 120 bp of DNA from MNase digestion and exhibit specific sequence preferences, suggesting a novel mechanism of nucleosome organization for the H2A.Z variant. PMID: 19246569

Both genetic and epigenetic features are likely to participate in targeting H2A.Z to distinct chromatin loci. PMID: 19261190

The nucleosome destabilizing effect of H2A.Z acetylation takes place synergistically with the acetylation of the rest of the core histones. PMID: 19385636

H2A.Z is incorporated into the promoter regions of estrogen receptor (ERalpha) target genes only upon gene induction, and that, in a cyclic pattern PMID: 19515975

show that upon gene induction, human H2A.Z associates with gene promoters and helps in recruiting the transcriptional machinery. PMID: 19834540

Both H2A.Z and H3.3 affect nucleosome positioning, either creating new positions or altering the relative occupancy of the existing nucleosome position space. Only H2A.Z-containing nucleosomes exhibit altered linker histone binding. PMID: 19856965